| Autor: |
Booth DR; Immunological Medicine Unit, Royal Postgraduate Medical School, Hammersmith Hospital, London, UK., Sunde M, Bellotti V, Robinson CV, Hutchinson WL, Fraser PE, Hawkins PN, Dobson CM, Radford SE, Blake CC, Pepys MB |
| Jazyk: |
angličtina |
| Zdroj: |
Nature [Nature] 1997 Feb 27; Vol. 385 (6619), pp. 787-93. |
| DOI: |
10.1038/385787a0 |
| Abstrakt: |
Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-beta fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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